Littérature scientifique sur le sujet « Ubiquitin-Specific Peptidase 1 »
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Articles de revues sur le sujet "Ubiquitin-Specific Peptidase 1"
Raimondi, Marzia, Daniela Cesselli, Carla Di Loreto, Francesco La Marra, Claudio Schneider et Francesca Demarchi. « USP1 (ubiquitin specific peptidase 1) targets ULK1 and regulates its cellular compartmentalization and autophagy ». Autophagy 15, no 4 (29 octobre 2018) : 613–30. http://dx.doi.org/10.1080/15548627.2018.1535291.
Texte intégralZhang, Jinghui, Chenchang Liu et Guofeng You. « Ubiquitin-specific peptidase 8 regulates the trafficking and stability of the human organic anion transporter 1 ». Biochimica et Biophysica Acta (BBA) - General Subjects 1864, no 12 (décembre 2020) : 129701. http://dx.doi.org/10.1016/j.bbagen.2020.129701.
Texte intégralShanmugam, Ilanchezhian, Mohammad Abbas, Farhan Ayoub, Susan Mirabal, Manal Bsaili, Erin K. Caulder, David M. Weinstock, Alan E. Tomkinson, Robert Hromas et Monte Shaheen. « Ubiquitin-specific Peptidase 20 Regulates Rad17 Stability, Checkpoint Kinase 1 Phosphorylation and DNA Repair by Homologous Recombination ». Journal of Biological Chemistry 289, no 33 (12 juin 2014) : 22739–48. http://dx.doi.org/10.1074/jbc.m114.550459.
Texte intégralAttaix, Didier, Sophie Ventadour, Audrey Codran, Daniel Béchet, Daniel Taillandier et Lydie Combaret. « The ubiquitin–proteasome system and skeletal muscle wasting ». Essays in Biochemistry 41 (1 octobre 2005) : 173–86. http://dx.doi.org/10.1042/bse0410173.
Texte intégralNakae, Aya, Michiko Kodama, Toru Okamoto, Makoto Tokunaga, Hiroko Shimura, Kae Hashimoto, Kenjiro Sawada et al. « Ubiquitin specific peptidase 32 acts as an oncogene in epithelial ovarian cancer by deubiquitylating farnesyl-diphosphate farnesyltransferase 1 ». Biochemical and Biophysical Research Communications 552 (mai 2021) : 120–27. http://dx.doi.org/10.1016/j.bbrc.2021.03.049.
Texte intégralOgawa, Masahiro, Tomoya Kitakaze, Naoki Harada et Ryoichi Yamaji. « Female-specific regulation of skeletal muscle mass by USP19 in young mice ». Journal of Endocrinology 225, no 3 (21 avril 2015) : 135–45. http://dx.doi.org/10.1530/joe-15-0128.
Texte intégralYu, Zhongxia, Hui Song, Mutian Jia, Jintao Zhang, Wenwen Wang, Qi Li, Lining Zhang et Wei Zhao. « USP1–UAF1 deubiquitinase complex stabilizes TBK1 and enhances antiviral responses ». Journal of Experimental Medicine 214, no 12 (14 novembre 2017) : 3553–63. http://dx.doi.org/10.1084/jem.20170180.
Texte intégralHu, Bin, Chunhua Ge et Chunqing Zhu. « Ubiquitin-specific peptidase 18 negatively regulates and inhibits lipopolysaccharide-induced sepsis by targeting transforming growth factor-β-activated kinase 1 activity ». International Immunology 33, no 9 (11 juin 2021) : 461–68. http://dx.doi.org/10.1093/intimm/dxab029.
Texte intégralYasunaga, J., F. C. Lin, X. Lu et K. T. Jeang. « Ubiquitin-Specific Peptidase 20 Targets TRAF6 and Human T Cell Leukemia Virus Type 1 Tax To Negatively Regulate NF- B Signaling ». Journal of Virology 85, no 13 (27 avril 2011) : 6212–19. http://dx.doi.org/10.1128/jvi.00079-11.
Texte intégralJingjing, Wu, Guo Wenzheng, Wen Donghua, Hou Guangyu, Zhou Aiping et Wu Wenjuan. « Deubiquitination and stabilization of programmed cell death ligand 1 by ubiquitin-specific peptidase 9, X-linked in oral squamous cell carcinoma ». Cancer Medicine 7, no 8 (10 juillet 2018) : 4004–11. http://dx.doi.org/10.1002/cam4.1675.
Texte intégralThèses sur le sujet "Ubiquitin-Specific Peptidase 1"
Cataldo, Francesca. « Role of calpain in USP1 stability regulation and genome integrity maintenance ». Doctoral thesis, Università degli studi di Trieste, 2012. http://hdl.handle.net/10077/7860.
Texte intégralThe calpains are a family of intracellular cysteine proteases, among which the best studied isoforms, micro- (CAPN1) and milli-calpain (CAPN2), are heterodimers consisting of a catalytic subunit and a common regulatory subunit, CAPNS1, required for function. Calpain is involved in many processes important for cancer biology, such as autophagy, indeed in calpain-depleted cells autophagy is impaired, with a subsequent increase in apoptosis sensitivity. Calpain is also important in all the stages of the stress response. A proteomic approach was employed for the identification of novel CAPNS1 interacting proteins. Proteins immunoprecipitating with endogenous CAPNS1 in HT1080 cell lysates were analyzed by Mass Spectrometry. We identified novel partners among which the deubiquitinating enzyme USP1, a key regulator of the DNA damage response and genome integrity maintenance via its specific action on FANCD2, involved in DNA repair and protection from chromosome instability, and PCNA, involved in the regulation of translesion DNA synthesis (TLS), that bypasses DNA lesions with low stringency basepairing requirements. We performed co-IP assays in lysates of 293T cells and confirmed that the interaction was specific. Furhermore, we observed that calpain is able to bind a USP1 C-terminal deleted mutant, suggesting that USP1 first 523 aminoacids were sufficient for the binding. To understand what is the effect exerted by calpain upon USP1, we depleted calpain activity in a series of cell lines, and followed the fate of endogenous USP1. We transfected CAPNS1 specific siRNAs, or treated cells with a specific inhibitor of calpain, and we observed a strong decrease in USP1 protein levels. This effect should be at a post-transcriptional level, since any significant change in USP1 mRNA levels is detected. We also obtained the same result by transfecting a siRNA specific for CAPN1, the gene encoding for the catalytic subunit micro-calpain. Moreover, we studied the role of calpain in the PCNA-mediated switch between high fidelity replication and TLS upon UV irradiation. In mouse embryonic fibroblasts knockout for CAPNS1, USP1 downregulation is coupled to an increase in PCNA monoubiquitination. Moreover, CAPNS1-depleted U2OS cells showed an increase in the percentage of nuclei containing PCNA-induced foci upon UV irradiation. Since we demonstrated that calpain can modulate an important regulator of DNA damage response such as USP1, we investigated if calpain could have a role in genome integrity maintenance. CAPNS1 depleted cells showed a reduced rescue in DNA repair compared to control cells, suggesting that increased levels in PCNA monoubiquitination could lead to an increased amount of errore-prone TLS. Calpain plays an important role in autophagy, so we asked if USP1 degradation in absence of calpain activity could involve autophagic pathways. We first blocked macroautophagy by silencing ATG5, and we observed that USP1 was downregulated, suggesting that the depletion of ATG5 could lead to an increased activity of other degradation pathways. To impaire chaperone-mediated autophagy (CMA), we silenced a protein important for autophagosome formation, LAMP-2A. Also in this case we observed a decrease in USP1 protein levels, thus suggesting that USP1 is alternatively degraded by different pathways. However, we observed that USP1 is stabilized upon inhibition of lysosomal enzymes, suggesting that USP1 may be degraded in the lysosome. To better understand the mechanism by which calpain affect USP1 stability we search for an effect of calpain upon USP1 co-factor and activator UAF1/WDR48. CAPNS1-depleted cells showed WDR48 downregulation, but WDR48 overexpression only partially rescue USP1 protein levels in this cells. Furthermore, we provided evidences that calpain regulation of p35/p25 activator of Cdk5 can affect Cdh1 phosphorylation and thus APC/Cdh1 activity, leading to a regulation of USP1 stabilization. In conclusion, we identified USP1 as a novel interactor of calpain, and we found that calpain is important for USP1 stability, since in its absence USP1 is downregulated. The importance of this novel regulation is strengthened by the recent findings that unveiled a role of USP1 in maintenance of a mesenchymal stem cell program in osteosarcoma, and thus placing calpain in a crucial regulatory position for cancer development.
XXIV Ciclo
1983
Chapitres de livres sur le sujet "Ubiquitin-Specific Peptidase 1"
Békés, Miklós, et Tony T. Huang. « Ubiquitin-specific Peptidase 1 ». Dans Handbook of Proteolytic Enzymes, 2079–85. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-382219-2.00468-3.
Texte intégralBékés, Miklós. « Ubiquitin-Specific Peptidase 10 ». Dans Handbook of Proteolytic Enzymes, 2076–79. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-382219-2.00467-1.
Texte intégralJones, Amanda, Chao Xu, Jinrong Min et Hengbin Wang. « Ubiquitin Specific Peptidase 16 ». Dans Handbook of Proteolytic Enzymes, 2090–94. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-382219-2.00470-1.
Texte intégralActes de conférences sur le sujet "Ubiquitin-Specific Peptidase 1"
Liu, Xi, Yun Lu, Weiguo Hu, Zibo Chen, Lisa M. Mustachio, Jason Roszik, Lin Zheng et al. « Abstract 2399 : Loss of ubiquitin-specific peptidase 18 (USP18) destabilizes the regulator of thermogenesis uncoupling protein-1 (UCP-1) and represses lung cancer growth ». Dans Proceedings : AACR Annual Meeting 2018 ; April 14-18, 2018 ; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-2399.
Texte intégralLiu, Xi, Yun Lu, Lin Zheng, David J. Sekula, Sarah J. Freemantle et Ethan Dmitrovsky. « Abstract 24 : Loss of ubiquitin-specific peptidase 18 (USP18) causes cold sensitive mice by destabilizing the critical regulator of thermogenesis : uncoupling protein-1 (UCP-1) ». Dans Proceedings : AACR 107th Annual Meeting 2016 ; April 16-20, 2016 ; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-24.
Texte intégralSingh, Mayank, Amy C. Burrows, Andrew Dickson, Komal Komal, Debjani Pal et Matthew K. Summers. « Abstract 496 : Ubiquitin specific peptidases 37 promotes constitutive replication fork movement by stabilizing Chk1 via its deubiquitination ». Dans Proceedings : AACR Annual Meeting 2017 ; April 1-5, 2017 ; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-496.
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